ID E3M7M0_CAERE Unreviewed; 908 AA.
AC E3M7M0;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 79.
DE RecName: Full=10-formyltetrahydrofolate dehydrogenase {ECO:0000256|PIRNR:PIRNR036489};
DE EC=1.5.1.6 {ECO:0000256|PIRNR:PIRNR036489};
GN ORFNames=CRE_12553 {ECO:0000313|EMBL:EFO93696.1}, FL81_05399
GN {ECO:0000313|EMBL:POM44970.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|EMBL:EFO93696.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|EMBL:EFO93696.1};
RG The Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:POM44970.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX356 {ECO:0000313|EMBL:POM44970.1};
RX PubMed=26114425; DOI=10.1371/journal.pgen.1005323;
RA Fierst J.L., Willis J.H., Thomas C.G., Wang W., Reynolds R.M.,
RA Ahearne T.E., Cutter A.D., Phillips P.C.;
RT "Reproductive Mode and the Evolution of Genome Size and Structure in
RT Caenorhabditis Nematodes.";
RL PLoS Genet. 11:e1005323-e1005323(2015).
RN [4] {ECO:0000313|EMBL:POM44970.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX356 {ECO:0000313|EMBL:POM44970.1};
RX PubMed=26394399; DOI=10.1371/journal.pgen.1005497;
RA Fierst J.L., Willis J.H., Thomas C.G., Wang W., Reynolds R.M.,
RA Ahearne T.E., Cutter A.D., Phillips P.C.;
RT "Correction: Reproductive Mode and the Evolution of Genome Size and
RT Structure in Caenorhabditis Nematodes.";
RL PLoS Genet. 11:e1005497-e1005497(2015).
RN [5] {ECO:0000313|EMBL:POM44970.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PX356 {ECO:0000313|EMBL:POM44970.1};
RA Banno H., Chua N.-H.;
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-10-formyltetrahydrofolate + H2O + NADP(+) = (6S)-5,6,7,8-
CC tetrahydrofolate + CO2 + H(+) + NADPH; Xref=Rhea:RHEA:10180,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:195366; EC=1.5.1.6;
CC Evidence={ECO:0000256|ARBA:ARBA00036910};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10181;
CC Evidence={ECO:0000256|ARBA:ARBA00036910};
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the aldehyde
CC dehydrogenase family. ALDH1L subfamily. {ECO:0000256|ARBA:ARBA00007995,
CC ECO:0000256|PIRNR:PIRNR036489}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the GART family.
CC {ECO:0000256|ARBA:ARBA00010978, ECO:0000256|PIRNR:PIRNR036489}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS268427; EFO93696.1; -; Genomic_DNA.
DR EMBL; LFJK02000008; POM44970.1; -; Genomic_DNA.
DR RefSeq; XP_003107797.1; XM_003107749.1.
DR AlphaFoldDB; E3M7M0; -.
DR STRING; 31234.E3M7M0; -.
DR EnsemblMetazoa; CRE12553.1; CRE12553.1; WBGene00062509.
DR GeneID; 9828600; -.
DR KEGG; crq:GCK72_014036; -.
DR CTD; 9828600; -.
DR eggNOG; KOG2452; Eukaryota.
DR HOGENOM; CLU_014974_0_0_1; -.
DR OMA; NEQVFMA; -.
DR OrthoDB; 2291791at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016155; F:formyltetrahydrofolate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0009258; P:10-formyltetrahydrofolate catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR CDD; cd08703; FDH_Hydrolase_C; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.10.25.10; Formyl transferase, C-terminal domain; 1.
DR Gene3D; 3.40.50.170; Formyl transferase, N-terminal domain; 1.
DR InterPro; IPR011407; 10_FTHF_DH.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR005793; Formyl_trans_C.
DR InterPro; IPR037022; Formyl_trans_C_sf.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR011034; Formyl_transferase-like_C_sf.
DR InterPro; IPR001555; GART_AS.
DR InterPro; IPR009081; PP-bd_ACP.
DR PANTHER; PTHR11699:SF190; 10-FORMYLTETRAHYDROFOLATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR Pfam; PF02911; Formyl_trans_C; 1.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR PIRSF; PIRSF036489; 10-FTHFDH; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR SUPFAM; SSF50486; FMT C-terminal domain-like; 1.
DR SUPFAM; SSF53328; Formyltransferase; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00373; GART; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR036489};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563,
KW ECO:0000256|PIRNR:PIRNR036489};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR036489,
KW ECO:0000256|RuleBase:RU003345};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008281}.
FT DOMAIN 328..402
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT ACT_SITE 112
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-1"
FT ACT_SITE 679
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 679
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-1"
FT ACT_SITE 713
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-1"
FT BINDING 94..96
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-2"
FT BINDING 148
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-2"
FT BINDING 603..606
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 656..657
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 763
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT BINDING 810..812
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-3"
FT SITE 148
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR036489-4"
SQ SEQUENCE 908 AA; 99460 MW; A37A04A874D80B33 CRC64;
MKIAIIGQSA FGVDVYKELR KNGHEVVVVF TIPDKNGRED LLAIEAAKDG VPVQKPARWR
KKNPETGKFE TLPEMLELYK SYNAELNVLP FCTQFIPLEI TEAPPKKSII YHPSILPKHR
GASAINWTLI EGDEEAGLSI FWADDGLDTG PILLQKKCKV EENDTLNTLY KRFLYPAGVA
AVAESVELIA SGKAPRIVQP EEGASYEPYI TTKPELAQID WSKPQRQLHN FIRGNDKVPG
AWAILNGEKV SFFGSKLWKP KKLPDDAVEV AVSEVPGGKV LVEDRGLLLP GSDGKWVIVD
TVKIGTKMIP ASKYGQGADQ VQELVLTDEE KETVAKLKKI WAGILKSQVS SDTDFFESGA
SSADVTRLVE EIKFNTGAEL ESGHIYSGPT LGENIDIVIR NLRGEGGLSV SYDPIVLNVN
NMELKFPHEQ FIDGKFVGSS DGRTFQTINP ATEKPICALP LATVADVDRA VRAAKKAFER
GEWRQMSARE RGKRLYRLAE LMEEHKEELA TLESLDAGAV YTLALKTHVG MSIDVWRYFA
GWCDKIQGKT IPISNARPNK NLCLTLREPI GVVGLITPWN YPLMMLSWKM AACLAAGNTV
VHKPAQVTPL TALKFAELSV LAGIPPGVIN IVTGSGSLVG NRLTAHPDVR KIGFTGSTEI
GATVMESCAK SNIKKVSLEL GGKSPLIIFA DADLEKAVKQ ACGAVFFNKG ENCIAAGRVF
IAKSIHDDFV KKLVEEAKQY QIGDPLDRST NHGPQNHLAH LNKLVEYVEN AVRDGAKVEI
GGKRLEREGL YFPPTILSNI DDENFAASEE SFGPIMCISS FDDDDVEDVL RRANDTEFGL
AAGVFTRDAS KSLRVAEALH AGTVFVNTYQ KTDVAAPFGG FKQSGFGKDM GEEALNEYLV
TKTITIEY
//
